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MRH4_LODEL
ID   MRH4_LODEL              Reviewed;         603 AA.
AC   A5E5F7;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MRH4; ORFNames=LELG_04846;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in mitochondrial RNA
CC       metabolism. Required for maintenance of mitochondrial DNA (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. MRH4 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH981530; EDK46665.1; -; Genomic_DNA.
DR   RefSeq; XP_001524033.1; XM_001523983.1.
DR   AlphaFoldDB; A5E5F7; -.
DR   SMR; A5E5F7; -.
DR   STRING; 379508.A5E5F7; -.
DR   PRIDE; A5E5F7; -.
DR   EnsemblFungi; EDK46665; EDK46665; LELG_04846.
DR   GeneID; 5231117; -.
DR   KEGG; lel:LELG_04846; -.
DR   VEuPathDB; FungiDB:LELG_04846; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   HOGENOM; CLU_003041_18_0_1; -.
DR   InParanoid; A5E5F7; -.
DR   OMA; FHALKMQ; -.
DR   OrthoDB; 1223767at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Transit peptide.
FT   TRANSIT         1..71
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           72..603
FT                   /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT                   /id="PRO_0000294673"
FT   DOMAIN          193..409
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          443..603
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           151..158
FT                   /note="Q motif"
FT   MOTIF           357..360
FT                   /note="DEAD box"
FT   BINDING         206..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   603 AA;  67375 MW;  24FC0A62B4CEFB59 CRC64;
     MISTGLPLFT LSKICHNCFF KQTRSLSRYS SKDKVKGRRR LLPRPNTEKF NSARSGVGVG
     VGNGAGAGAR VGVGAGAGSV AAKVFESGNF SQLHNNGLSK QAQTAGLDLK QKITSFDQLK
     VFPSVREAMI KEIKSQYNLK GPQHSSIDDV VIKPTPVQIA AIRKINQTRK IKVAKNLDEM
     SEGERIQIEL QTKNEEQKTK IFTVAAETGS GKTWAYLANI MSKLKEDDYK WFNQSPEAYN
     SFKSSEQVRS VILLPTHELV EQVYETLKRA NSFLLEYENV PLQYKEFLNL PEHHTLGLSI
     AKLSHGDAPI NVYKQLRNRG KIDILITTPG KITSFSKLES IDRPFKIFKS IRYCVIDEAD
     TLFDDSFLKD TTAVVKNFPK LLDLILVSAT IPKEFEKTLL RLFPDQKSLI RVATPSLHKI
     SKNIKVMTLD ADLAPYNGSK TRCLAQAIYA ISKDGTEHNH VKRIIIFVNE KAEVDGLVDL
     LQSKYHIRRE DICGISGSVN VGDRKDYLEP FLKPAQLLED DVDQSKIKIL VTTDLLARGM
     NFIGIKNVIL MGLPKSSVEL VHRLGRTGRM NQLGRVFIIV DKKSRKSWVK GLGSAIMKGS
     RIG
 
 
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